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  1. 紀要
  2. Tumor Research
  3. Vol.41

Proteins interacting with CHFR, mitotic-checkpoint ubiquitin ligase

https://doi.org/10.15114/tr.41.23
https://doi.org/10.15114/tr.41.23
155c03e3-072d-475c-9e95-38e1ef5a5636
名前 / ファイル ライセンス アクション
n0041409341123.pdf n0041409341123.pdf (533.9 kB)
Item type 紀要論文 / Departmental Bulletin Paper(1)
公開日 2019-07-31
タイトル
タイトル Proteins interacting with CHFR, mitotic-checkpoint ubiquitin ligase
言語 en
言語
言語 eng
キーワード
言語 en
主題Scheme Other
主題 Ubiquitination
キーワード
言語 en
主題Scheme Other
主題 Microtubule inhibitor
キーワード
言語 en
主題Scheme Other
主題 Cell cycle
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ departmental bulletin paper
ID登録
ID登録 10.15114/tr.41.23
ID登録タイプ JaLC
著者 Mita, Hiroaki

× Mita, Hiroaki

Mita, Hiroaki

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Toyota, Minoru

× Toyota, Minoru

Toyota, Minoru

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Sasaki, Yasushi

× Sasaki, Yasushi

Sasaki, Yasushi

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Suzuki, Hiromu

× Suzuki, Hiromu

Suzuki, Hiromu

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Idogawa, Masashi

× Idogawa, Masashi

Idogawa, Masashi

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Kashima, Lisa

× Kashima, Lisa

Kashima, Lisa

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Tokino, Takashi

× Tokino, Takashi

Tokino, Takashi

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抄録
内容記述タイプ Abstract
内容記述 Cell cycle progression is monitored by checkpoint mechanisms to ensure the integrity of the genome. CHFR which contains a RING domain and has ubiquitin ligase activity, a novel mitotic checkpoint gene, delays chromosome condensation in cells treated with microtubule poisons. CHFR is inactivated by promoter methylation and point mutations in various human tumors, and cancer cells lacking CHFR are sensitive to microtubule inhibitors. However, few reports are available on the molecular mechanism that accounts for the link between the sensitivity of cancer cells to microtubule inhibitors and the physiological function of CHFR. In the present study, we isolated cellular proteins capable of interacting with CHFR using yeast two-hybrid method to clarify the function of CHFR. As a result of the screening, we isolated canonical and noncanonical E2 ubiquitin conjugating enzymes as CHFR interacting proteins, which are involved in proteolytic and non-proteolytic ubiquitination respectively. This raises the possibility that CHFR is switching canonical and noncanonical ubiquitination depending on the situation of cells. On the other hand, we isolated gadd34 which interacted with the FHA domain of CHFR by two-hybrid screen. Coexpression in mammalian cells showed that gadd34 interacted with the FHA domain of CHFR, but gadd34 is not the substrate for CHFR, rather it promoted autoubiquitination of CHFR. Furthermore, CHFR moved, in part, from nucleus to cytoplasm in the presence of microtubule inhibitor docetaxel, which enabled colocalization of CHFR and gadd34 in cytoplasm. This colocalization was followed by cell death. These findings suggest that gadd34 and CHFR cooperate to mediate cell death in response to mitotic stress.
書誌情報 Tumor Research
en : Tumor Research

巻 41, p. 23-41, 発行日 2006
ISSN
収録物識別子タイプ ISSN
収録物識別子 0041-4093
著者版フラグ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
出版者
出版者 Sapporo Medical University
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